Chlorine in PDB 4gwe: W116L-OYE1 Complexed with (R)-Carvone

All present enzymatic activity of W116L-OYE1 Complexed with (R)-Carvone:
1.6.99.1;

The structure of W116L-OYE1 Complexed with (R)-Carvone, PDB code: 4gwe was solved by Y.A.Pompeu, J.D.Stewart, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.16 / 1.45
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	140.780, 140.780, 42.760, 90.00, 90.00, 90.00
R / Rfree (%)	11.5 / 14.5

The structure of W116L-OYE1 Complexed with (R)-Carvone also contains other interesting chemical elements:

Magnesium	(Mg)	2 atoms
Sodium	(Na)	2 atoms

The binding sites of Chlorine atom in the W116L-OYE1 Complexed with (R)-Carvone (pdb code 4gwe). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the W116L-OYE1 Complexed with (R)-Carvone, PDB code: 4gwe:

Chlorine binding site 1 out of 1 in the W116L-OYE1 Complexed with (R)-Carvone


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of W116L-OYE1 Complexed with (R)-Carvone within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl407 b:19.7 occ:1.00 ND2 A:ASN126 3.2 13.5 1.0 O A:HOH692 3.2 13.8 1.0 N A:ASP83 3.3 11.2 1.0 O A:HOH1008 3.7 52.0 1.0 O A:HOH986 3.7 46.9 1.0 CD2 A:PHE123 3.8 15.9 1.0 CA A:TYR82 3.8 10.2 1.0 CE2 A:PHE123 3.9 18.5 1.0 O A:HOH968 4.0 35.5 1.0 C A:TYR82 4.0 10.7 1.0 CB A:ASP83 4.0 13.9 1.0 CA A:ASP83 4.2 12.0 1.0 CG A:ASP83 4.2 15.6 1.0 OD2 A:ASP83 4.3 18.4 1.0 CG A:ASN126 4.3 14.2 1.0 O A:GLY81 4.4 11.7 1.0 O A:HOH714 4.5 21.9 1.0 CB A:TYR82 4.5 10.4 1.0 OD1 A:ASN126 4.7 16.8 1.0 OD1 A:ASP83 4.9 15.9 1.0 N A:ASN84 4.9 10.4 1.0 CD1 A:TYR82 4.9 10.7 1.0 N A:TYR82 4.9 10.6 1.0

Y.A.Pompeu, B.Sullivan, J.D.Stewart. X‑Ray Crystallography Reveals How Subtle Changes Control the Orientation of Substrate Binding in An Alkene Reductase Acs Catalysis V. 3 2376 2013.
ISSN: ESSN 2155-5435
DOI: 10.1021/CS400622E